|Isolation and purification of glutathione s-transferases from Brachionus plicatilis and B. Calyciflorus (Rotifera)|
Bowman, B.P.; Snell, T.W.; Cochrane, B.J. (1990). Isolation and purification of glutathione s-transferases from Brachionus plicatilis and B. Calyciflorus (Rotifera). Comp. Biochem. Physiol. (B Biochem. Mol. Biol.) 95(3): 619-624
In: Comparative Biochemistry and Physiology. Part B. Biochemistry and Molecular Biology. Pergamon: Oxford. ISSN 1096-4959, more
|Authors|| || Top |
- Bowman, B.P.
- Snell, T.W.
- Cochrane, B.J.
1. The enzyme glutathione S-transferase (GST), a critical element in xenobiotic metabolism, was isolated from the marine rotifer Brachionus plicatilis and its freshwater congener B. calyciflorus. 2. In B. plicatilis, GST comprised 4.2% of cytosolic protein and was present as three separate isozymes with mol. wts 30,000, 31,400 and 33,700. Specific activity of crude homogenates was 56 nmol min-1 mg-1 protein, while that of affinity chromatography purified GST was 1850. 3. In B. calyciflorus, GST was present as two isozymes with mol. wts of 26,300 and 28,500, representing 1.0% of cytosolic protein. Crude GST specific activity was 1750 nmol min-1 mg-1 protein and purified was 72,400. 4. Rotifer GSTs are unusual because they are monomers whereas all other animals thus far investigated posses dimeric GSTs.